位置:首页 > 蛋白库 > ACE2_CANAL
ACE2_CANAL
ID   ACE2_CANAL              Reviewed;         783 AA.
AC   Q59RR0; A0A1D8PTH9;
DT   26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 2.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Cell wall transcription factor ACE2;
GN   Name=ACE2; OrderedLocusNames=CAALFM_CR07440WA;
GN   ORFNames=CaO19.13543, CaO19.6124;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN   [4]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15255906; DOI=10.1111/j.1365-2958.2004.04185.x;
RA   Kelly M.T., MacCallum D.M., Clancy S.D., Odds F.C., Brown A.J., Butler G.;
RT   "The Candida albicans CaACE2 gene affects morphogenesis, adherence and
RT   virulence.";
RL   Mol. Microbiol. 53:969-983(2004).
RN   [5]
RP   FUNCTION.
RX   PubMed=16998073; DOI=10.1128/ec.00155-06;
RA   Mulhern S.M., Logue M.E., Butler G.;
RT   "Candida albicans transcription factor Ace2 regulates metabolism and is
RT   required for filamentation in hypoxic conditions.";
RL   Eukaryot. Cell 5:2001-2013(2006).
RN   [6]
RP   FUNCTION.
RX   PubMed=18843050; DOI=10.1091/mbc.e08-03-0272;
RA   Song Y., Cheon S.A., Lee K.E., Lee S.Y., Lee B.K., Oh D.B., Kang H.A.,
RA   Kim J.Y.;
RT   "Role of the RAM network in cell polarity and hyphal morphogenesis in
RT   Candida albicans.";
RL   Mol. Biol. Cell 19:5456-5477(2008).
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=19528234; DOI=10.1128/mcb.01502-08;
RA   Wang A., Raniga P.P., Lane S., Lu Y., Liu H.;
RT   "Hyphal chain formation in Candida albicans: Cdc28-Hgc1 phosphorylation of
RT   Efg1 represses cell separation genes.";
RL   Mol. Cell. Biol. 29:4406-4416(2009).
RN   [8]
RP   FUNCTION.
RX   PubMed=21335533; DOI=10.1128/ec.00289-10;
RA   Stichternoth C., Fraund A., Setiadi E., Giasson L., Vecchiarelli A.,
RA   Ernst J.F.;
RT   "Sch9 kinase integrates hypoxia and CO2 sensing to suppress hyphal
RT   morphogenesis in Candida albicans.";
RL   Eukaryot. Cell 10:502-511(2011).
RN   [9]
RP   FUNCTION.
RX   PubMed=22359502; DOI=10.1371/journal.ppat.1002525;
RA   Finkel J.S., Xu W., Huang D., Hill E.M., Desai J.V., Woolford C.A.,
RA   Nett J.E., Taff H., Norice C.T., Andes D.R., Lanni F., Mitchell A.P.;
RT   "Portrait of Candida albicans adherence regulators.";
RL   PLoS Pathog. 8:E1002525-E1002525(2012).
RN   [10]
RP   FUNCTION.
RX   PubMed=23243062; DOI=10.1128/ec.00278-12;
RA   Heilmann C.J., Sorgo A.G., Mohammadi S., Sosinska G.J., de Koster C.G.,
RA   Brul S., de Koning L.J., Klis F.M.;
RT   "Surface stress induces a conserved cell wall stress response in the
RT   pathogenic fungus Candida albicans.";
RL   Eukaryot. Cell 12:254-264(2013).
CC   -!- FUNCTION: Transcription factor involved in the RAM (regulation of ACE2
CC       transcription factor and polarized morphogenesis) signaling network
CC       that regulates polarized morphogenesis. Regulates expression of genes
CC       involved in cell separation such as CHT3, DSE1, and SCW11; or other
CC       cell wall genes such as ASH1, DSE4, PIR1, PRY2, and RME1. Required for
CC       regulation of morphogenesis, cell separation, adherence, biofilm
CC       formation, invasion, as well as virulence in a mouse model of
CC       infection. {ECO:0000269|PubMed:15255906, ECO:0000269|PubMed:16998073,
CC       ECO:0000269|PubMed:18843050, ECO:0000269|PubMed:21335533,
CC       ECO:0000269|PubMed:22359502, ECO:0000269|PubMed:23243062}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15255906,
CC       ECO:0000269|PubMed:19528234}. Note=Localized in the nuclei of daughter
CC       cells.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP017630; AOW31437.1; -; Genomic_DNA.
DR   RefSeq; XP_712331.2; XM_707238.2.
DR   AlphaFoldDB; Q59RR0; -.
DR   SMR; Q59RR0; -.
DR   BioGRID; 1229088; 10.
DR   STRING; 237561.Q59RR0; -.
DR   PRIDE; Q59RR0; -.
DR   GeneID; 3646034; -.
DR   KEGG; cal:CAALFM_CR07440WA; -.
DR   CGD; CAL0000191878; ACE2.
DR   VEuPathDB; FungiDB:CR_07440W_A; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   HOGENOM; CLU_022817_0_0_1; -.
DR   InParanoid; Q59RR0; -.
DR   OrthoDB; 1015026at2759; -.
DR   PHI-base; PHI:331; -.
DR   PRO; PR:Q59RR0; -.
DR   Proteomes; UP000000559; Chromosome R.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 2.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   SUPFAM; SSF57667; SSF57667; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE   4: Predicted;
KW   Cell adhesion; Cell wall biogenesis/degradation; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Transcription; Transcription regulation;
KW   Virulence; Zinc; Zinc-finger.
FT   CHAIN           1..783
FT                   /note="Cell wall transcription factor ACE2"
FT                   /id="PRO_0000422792"
FT   ZN_FING         649..673
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         679..701
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          166..195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          219..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          355..452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          474..497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          535..624
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..254
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..299
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        355..409
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        479..497
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        535..614
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   783 AA;  90571 MW;  8256A2F177F761A0 CRC64;
     MHWKFSNFRK YHLSFHLNLF DLSLFFISFY CFPILYICFF NQVHSFRSTQ PSLIMNKFDL
     FDDYSTKGST IPLPNENFDQ LFLSSEANDM EFLFNETLMG LQDLDVPSGY GIPQNTINND
     FQHTPNKSKS HSRQYSGTAI FGFADHNKDL SINGVNNDLC KQSNKAINTQ SVSPGELLKR
     SRGSQTPTPT SALPDTAQDI LDFNFEEKPI LLLEEDELEE EKHKQQQRMM TQSSPLKRVT
     TPSQSPFVQQ PQTMKQRKPH KKTNEYIVAN ENPNSYKFPP SPSPTAKRQQ YPPSSPIPYN
     PKSDSVGGNS YSAKYLQSLN KTQQIEYVDD IEPLLQEDNN NMKYIPIPVQ EPMSYQKQKP
     VTPPLQSQND SQQLEPLKTP QPQPKQQQQQ QQPNNEQDKE FTANFNFNTF LPPPTPPNLI
     NGSPDWNSSP EPHSPSPGRL QPPQQISPIH QNLGAMGNNI NFYTPMYYEL PVQAEQPQPQ
     PQPHQQQHQQ QQHQPELQNT YQQIKHIQQQ QQMLQHQFHN QNNQLRQQHP NQFQNQNQNQ
     NQNQTKTPYS QQSQFSPTHS NFNLSPAKQL NSNVGSMHLS PLKKQLPNTP TKQPPVTIEW
     SPVISPNSKQ PLHKQIKESS PRRRIKKTSL LPPGELDNYW TGPDEDKIYT CTYKNCGKKF
     TRRYNVRSHI QTHLSDRPFG CQFCPKRFVR QHDLNRHVKG HIEARYSKCP CGKEFARLDA
     LRKHQDRNIC VGGNKNVISK PTKKKGTNNT QQQLLKTDTV VERIEKQLLQ EDKSVTEEFL
     MLQ
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024